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Rev
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rev
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HIV-1 Rev interacting protein, karyopherin alpha 2 (KPNA2), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with KPNA2 is decreased by RRE |
PubMed
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Tat
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tat
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Interaction of HIV-1 Tat with KPNA2 in T-cells is identified by a proteomic strategy based on affinity chromatography |
PubMed
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tat
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HIV-1 Tat peptide (amino-acids 47-57) binds to importin alpha and beta receptors |
PubMed
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Vpr
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vpr
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HIV-1 Vpr binds KPNA2; C-terminus changes conformation to a twisted beta-turn enabling binding to a minor KPNA2 nuclear localization. Vpr C-terminus can also bind major KPNA2 nuclear localization signal sites in an extended conformation in different ways. |
PubMed
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vpr
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HIV-1 Vpr interacts with both karyopherin alpha 1 and alpha 2 to facilitate nuclear import of the HIV-1 preintegration complex, however conflicting reports indicate it may also be imported by other mechanisms independently of karyopherin alpha 1 and 2 |
PubMed
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vpr
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Full-length Vpr interacts with RCH1 through its binding to the C-terminal domain (residues 404-529) of RCH1 |
PubMed
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vpr
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The nuclear import of Vpr is promoted by the addition of cytoplasmic extracts from macrophages but not of that from monocytes, and the nuclear import activity is lost with immunodepletion of importin alpha from the cytoplasmic extract |
PubMed
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vpr
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A small molecule hematoxylin, which suppresses Vpr-Importin alpha interaction, blocks Vpr nuclear entry in a dose-dependent manner |
PubMed
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vpr
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HIV-1 Vpr interacts with importin-alpha through alphaH1 (residues 17-34) and alphaH2 (residues 46-74); the interaction via alphaH1 is indispensable for the nuclear entry of Vpr, and residues 393-462 of importin-alpha promote entry of Vpr into the nucleus |
PubMed
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integrase
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gag-pol
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Karyopherin alpha and beta are reported to interact with HIV-1 integrase (IN) to facilitate nuclear import of IN, however a conflicting report indicates nuclear accumulation of IN does not involve karyopherin alpha, beta 1, or beta 2 mediated pathways |
PubMed
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gag-pol
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Ivermectin, an inhibitor of importin alpha/beta1, inhibits HIV-1 infection by blocking the HIV-1 Integrase interaction with importin alpha/beta1 for viral protein nuclear import |
PubMed
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gag-pol
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HIV-1 IN interacts with importin alpha by the BiFC assay and amino acids 161-173 in IN are required for the interaction with importin alpha |
PubMed
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gag-pol
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HIV-1 Rev disrupts both IN-TNPO3 and IN-importin alpha complexes |
PubMed
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gag-pol
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Some reports indicate a possible role for the interactions between karyopherin alpha and beta with HIV-1 integrase in the nuclear import of HIV-1 preintegration complexes (PIC), while other reports indicate integrase is not involved in PIC nuclear import |
PubMed
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gag-pol
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Karyopherin alpha binds to a bipartite nuclear localization signal in HIV-1 integrase (amino acids 186-189 and 211-219) |
PubMed
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matrix
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gag
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Nuclear import of HIV-1 preintegration complexes by karyopherin alpha is governed by phosphorylation of HIV-1 Matrix on tyrosine and serine, however the exact role of phosphorylation of the C-terminal tyrosine of Matrix has been debated |
PubMed
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gag
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HIV-1 Matrix increases intracellular ATP content, an effect hypothesized to support the ATP-dependent nuclear import of HIV-1 preintegration complexes by karyopherin alpha |
PubMed
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gag
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HIV-1 Vpr increases the affinity of karyopherin alpha to the HIV-1 Matrix nuclear localization signal, thereby mediating the nuclear import of HIV-1 preintegration complexes |
PubMed
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gag
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Hsp70 stimulates the binding of HIV-1 matrix to karyopherin alpha |
PubMed
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gag
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The role of HIV-1 Matrix during nuclear import of the HIV-1 preintegration complex has been controversial, however recent understanding indicates HIV-1 Matrix and Vpr proteins act in concert to facilitate nuclear import by binding to karyopherin alpha |
PubMed
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gag
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HIV-1 Matrix contains two nuclear localization signals (NLS) spanning amino acids 24-33 and 110-114 that are recognized by karyopherin alpha and mediate the nuclear import of HIV-1 preintegration complexes |
PubMed
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